ArticleMolecular & general genetics : MGG1993
The amiloride resistance gene, car1, of Schizosaccharomyces pombe.
Article in Molecular & general genetics : MGG, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 25 citations in OpenAlex.
- Amiloride uptake and toxicity in fission yeast are caused by the pyridoxine transporter encoded by bsu1+ (car1+).Eukaryotic cell · 2005Article
- Insertional mutagenesis based on illegitimate recombination in Schizosaccharomyces pombe.Nucleic acids research · 2000Article
- Identification of Saccharomyces cerevisiae genes conferring resistance to quinoline ring-containing antimalarial drugs.Antimicrobial agents and chemotherapy · 1998Article
- Proton-dependent multidrug efflux systems.Microbiological reviews · 1996Review
- Amino acid substitutions in membrane-spanning domains of Hol1, a member of the major facilitator superfamily of transporters, confer nonselective cation uptake in Saccharomyces cerevisiae.Journal of bacteriology · 1996Article
- Molecular cloning and characterization of a novel gene of Candida albicans, CDR1, conferring multiple resistance to drugs and antifungals.Current genetics · 1995Article
- Multidrug resistance in Candida albicans: disruption of the BENr gene.Antimicrobial agents and chemotherapy · 1995Article
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4 authors at 1 institution in 1 country.
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Abstract
Amiloride, an inhibitor of various sodium transporters, is toxic to Schizosaccharomyces pombe at low concentration in minimal but not in rich media. Amiloride-resistant mutants were isolated and shown to represent a new locus (car1 for changed amiloride resistance) on chromosome I. The car1 gene was cloned and sequenced. Sequence analysis revealed an open reading frame of 526 amino acids with a predicted molecular weight of 58,545 Da. It has 52% hydrophobic residues and belongs to the class of 12-transmembrane-domain transport proteins. Gene disruption of car1 results in increased amiloride resistance. car1 has sequence similarity to proteins from Candida associated with resistance to benomyl, methotrexate and cycloheximide. No single physiologically identifiable component of sodium transport appeared to be lost. We propose that car1 serves an uptake function, perhaps as a symport with an unknown substrate and this carrier may transport amiloride into the cell. Further, we suggest that amiloride toxicity at low concentrations is not due to its effect on sodium transport but, rather, depends on intracellular interference with an unknown biosynthetic pathway.
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